Arginine and Lysine interactions with π residues in metalloproteins

doi:10.6026/97320630008820

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Arginine and Lysine interactions with π residues in metalloproteins

Journal Article•DOI•

Arginine and Lysine interactions with π residues in metalloproteins

P. Anitha¹, Vaideeswaran Sivasakthi¹, P. Lavanya, Susmita Bag, K. M. Kumar, Anand Anbarasu, Sudha Ramaiah¹ - Show less +3 more•Institutions (1)

VIT University¹

11 Sep 2012-Bioinformation (Biomedical Informatics Publishing Group)-Vol. 8, Iss: 17, pp 820-826

TL;DR: The roles played by Arg and Lys (cationic side chains) interactions with π (Phe, Tyr or Trp) residues and their role in the structural stability of metalloproteins are analyzed.

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Abstract: Metalloproteins have many different functions in cells such as enzymes; signal transduction, transport and storage proteins. About one third of all proteins require metals to carry out their functions. In the present study we have analyzed the roles played by Arg and Lys (cationic side chains) interactions with π (Phe, Tyr or Trp) residues and their role in the structural stability of metalloproteins. These interactions might play an important role in the global conformational stability in metalloproteins. In spite of its lower natural occurrence (1.76%) the number of Trp residues involved in energetically significant interactions is higher in metalloproteins.

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Journal Article•DOI•

Cation–π Interactions in β-Lactamases: The Role in Structural Stability

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P. Lavanya¹, Sudha Ramaiah¹, Anand Anbarasu¹•Institutions (1)

VIT University¹

01 May 2013-Cell Biochemistry and Biophysics

TL;DR: The results indicate that cation–π interactions might play an important role in the global conformational stability of β-lactamases.

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Abstract: β-lactam group of antibiotics is the most widely used therapeutic molecules for treating bacterial infections. The main mode of bacterial resistance to β-lactams is by β-lactamases. In the present study, we report our results on the role of cation–π interactions in β-lactamases and their environmental preferences. The number of interactions formed by arginine is higher than lysine in the cationic group, while tyrosine is comparatively higher than phenylalanine and tryptophan in the π group. Our results indicate that cation–π interactions might play an important role in the global conformational stability of β-lactamases.

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14 citations

Journal Article•DOI•

Investigations on the role of π-π interactions and π-π networks in eNOS and nNOS proteins.

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Sivasakthi Vaideeswaran¹, Sudha Ramaiah¹•Institutions (1)

VIT University¹

01 Aug 2013-Bioorganic Chemistry

TL;DR: The influence of π-π interactions in eNOS and nNOS proteins in sequential separation, secondary structure involvement, solvent accessibility and stabilization centers has been evaluated.

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4 citations

Journal Article•DOI•

Contribution of cation–π interactions to the stability of Sm/LSm oligomeric assemblies

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Ivana D. Mucić¹, Milan Nikolić¹, Srđan Đ. Stojanović¹•Institutions (1)

University of Belgrade¹

01 Jul 2015-Protoplasma

TL;DR: Stabilization centers for these proteins showed that all the five residues found in cation-π interactions are important in locating one or more of such centers, and more than 50 % of the cation–π interacting residues are highly conserved.

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Abstract: In this work, we have analyzed the influence of cation–π interactions to the stability of Sm/LSm assemblies and their environmental preferences. The number of interactions formed by arginine is higher than lysine in the cationic group, while histidine is comparatively higher than phenylalanine and tyrosine in the π group. Arg–Tyr interactions are predominant among the various pairs analyzed. The furcation level of multiple cation–π interactions is much higher than that of single cation–π interactions in Sm/LSm interfaces. We have found hot spot residues forming cation–π interactions, and hot spot composition is similar for all aromatic residues. The Arg–Phe pair has the strongest interaction energy of −8.81 kcal mol−1 among all the possible pairs of amino acids. The extent of burial of the residue side-chain correlates with the ΔΔG of binding for residues in the core and also for hot spot residues cation–π bonded across the interface. Secondary structure of the cation–π residues shows that Arg and Lys preferred to be in strand. Among the π residues, His prefers to be in helix, Phe prefers to be in turn, and Tyr prefers to be in strand. Stabilization centers for these proteins showed that all the five residues found in cation–π interactions are important in locating one or more of such centers. More than 50 % of the cation–π interacting residues are highly conserved. It is likely that the cation–π interactions contribute significantly to the overall stability of Sm/LSm proteins.

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3 citations

Cites background or result from "Arginine and Lysine interactions wi..."

...These results are comparable with the results observed in β-lactamases (Lavanya et al. 2013), RNA-binding proteins (Anbarasu et al. 2007), immunoglobulin proteins (Tayubi and Sethumadhavan 2010), sugarbinding proteins (Elumalai et al. 2010), and metalloproteins (Anitha et al. 2012)....
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...2010), metalloproteins (Anitha et al. 2012), and therapeutic proteins (Shanthi et al....
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...…were not consistent with the results observed with cation–π pairs in β-lactamases (Lavanya et al. 2013), immunoglobulin proteins (Tayubi and Sethumadhavan 2010), sugar-binding proteins (Elumalai et al. 2010), metalloproteins (Anitha et al. 2012), and therapeutic proteins (Shanthi et al. 2009)....
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...This trend is similar to those observed in βlactamases (Lavanya et al. 2013), immunoglobulin proteins (Tayubi and Sethumadhavan 2010), sugar-binding proteins (Elumalai et al. 2010), metalloproteins (Anitha et al. 2012), and therapeutic proteins (Shanthi et al. 2009)....
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...…were consistent with the results observed with cation–π pairs in β-lactamases (Lavanya et al. 2013), immunoglobulin proteins (Tayubi and Sethumadhavan 2010), sugar-binding proteins (Elumalai et al. 2010), metalloproteins (Anitha et al. 2012), and therapeutic proteins (Shanthi et al. 2009)....
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